title: Protein phosphorylation in Streptomyces albus.
abstract: The phosphorylated proteins of Streptomyces albus, radioactively labeled with [32P]orthophosphate have been analyzed by gel electrophoresis and autoradiography. More than 10 protein species were found to be phosphorylated. With [32P]ATP as substrate cell free extracts phosphorylated endogenous proteins in vitro which were predominantly phosphorylated in vivo. From cell extract which exhibited active phosphorylated in vitro, a protein kinase has been partially purified. The kinase activity was identified in fractions corresponding to a 90 kDa protein.
authors.affiliation: Institute of Microbiology, Czechoslovak Academy of Sciences, Prague.
authors.forename: Z
authors.initials: Z
authors.lastname: Dobrová
authors.forename: M
authors.initials: M
authors.lastname: Jiresová
authors.forename: T
authors.initials: T
authors.lastname: Petrík
authors.forename: P
authors.initials: P
authors.lastname: Rysavý
authors.forename: J
authors.initials: J
authors.lastname: Náprstek
authors.forename: J
authors.initials: J
authors.lastname: Janecek
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D011494:Protein Kinases